ID   MANA_PIRSP              Reviewed;         606 AA.
AC   P55296;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase A;
DE            EC=3.2.1.78;
DE   AltName: Full=1,4-beta-D-mannan mannanohydrolase A;
DE   AltName: Full=Beta-mannanase A;
DE   Flags: Precursor;
GN   Name=MANA;
OS   Piromyces sp.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces; unclassified Piromyces.
OX   NCBI_TaxID=45796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7493964; DOI=10.1074/jbc.270.49.29314;
RA   Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J.;
RT   "The conserved noncatalytic 40-residue sequence in cellulases and
RT   hemicellulases from anaerobic fungi functions as a protein docking
RT   domain.";
RL   J. Biol. Chem. 270:29314-29322(1995).
CC   -!- FUNCTION: Hydrolyzes 1,4-beta linked polysaccharide backbones of
CC       mannans, one of the major hemicellulose components in hardwoods and
CC       softwoods. Shows very high activity against mannohexaose but not
CC       against mannopentaose and smaller mannooligosaccharides. The major
CC       products released from mannooligosaccharide hydrolysis are mannose and
CC       mannobiose. The reiterated 40 AA domain is involved in binding the
CC       cellulase-hemicellulase complex.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC         mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC   -!- DOMAIN: Consists of a catalytic N-terminal domain linked to a
CC       reiterated non-catalytic C-terminal domain.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
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DR   EMBL; X91857; CAA62968.1; -; mRNA.
DR   AlphaFoldDB; P55296; -.
DR   SMR; P55296; -.
DR   CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR   CAZy; GH26; Glycoside Hydrolase Family 26.
DR   CLAE; MAN26A_PIRSP; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1220.10; -; 3.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR009034; Dockerin_dom_fun_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR022790; GH26_dom.
DR   InterPro; IPR000805; Glyco_hydro_26.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR40079; PTHR40079; 1.
DR   Pfam; PF02013; CBM_10; 3.
DR   Pfam; PF16990; CBM_35; 1.
DR   Pfam; PF02156; Glyco_hydro_26; 1.
DR   PRINTS; PR00739; GLHYDRLASE26.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF64571; SSF64571; 3.
DR   PROSITE; PS51763; CBM10; 3.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Repeat; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..606
FT                   /note="Mannan endo-1,4-beta-mannosidase A"
FT                   /id="PRO_0000012174"
FT   DOMAIN          22..140
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          164..458
FT                   /note="GH26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   DOMAIN          491..527
FT                   /note="CBM10 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          530..566
FT                   /note="CBM10 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          569..605
FT                   /note="CBM10 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   REGION          472..489
FT                   /note="Linker"
FT   ACT_SITE        318
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        406
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         493
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
SQ   SEQUENCE   606 AA;  68055 MW;  79AAFEEFA2725D86 CRC64;
     MKSLNVILTL LSLIISVLSK KVYYEAEDGK LNGITVFKEL SGFSGKGYVG RFENPGNSVT
     VTVDAPATGM YDLSIIYCAN MGQKINSLTV NDQSVGDITF TENTKFETKD VGAVYLNKGK
     NTIGLVSSWG WMWVDAFVIN DAPNAAKDVS SKLNPTLVNP KAIPAAKKLY DFLKTNYGKR
     ILSGQVGAAG QAGDEGQEIQ RIQKATGKLP AVWNMDFIFE SNDCTWRPQN PDITEMAINW
     WKKYEGKGIM AAQWHWNIAG KTGDFAFYSK DTTFNLENAV TEGTWEYEKI IKDIDRVSGH
     IKKLQAVNMP LIWRPLHENN GDWFWWGNNP KACAKLWKIL YERMVNYHGL NNLIWLWNGN
     NDANTPVDYI DIIGVDIYAN DHGPQTTAYN THFDFYGGKK MVVLSENGRI PDIQQCVDQD
     VWWGYFQTWN SEFILQDSYH TDAQLKEYFN HKTVMNMDEL PSFNVDSYNG DSGSSHNGNS
     ESNSNTGNSD ECWSINLGYP CCIGDYVVTT DENGDWGVEN NEWCGIVHKS CWSEPLGYPC
     CVGNTVISAD ESGDWGVENN EWCGIVHKSC WAEFLGYPCC VGNTVISTDE FGDWGVENDD
     WCGILN